Abstract
Lactoferrin was first discovered in bovine milk in 19391. It was later found in high concentration in human milk2. Lactoferrin is a glycoprotein with a molecular weight of 78,000 and has the capacity to bind two ferric ions concomitant with bicarbonate or carbonate ions. The primary structure3 as well as the glycan structure4 have been documented and the tertiary structure has been elucidated by X-ray crystallography5. The protein consists of two lobes, each binding one iron atom and having one glycan; because of the similarity between the two lobes, the molecule is believed to be the result of an early gene duplication3. Lactoferrin is sometimes referred to as lactotransferrin3,4. However, even if lactoferrin and transferrin have some similar physicochemical properties, they are products of different genes and their biological functions are different.
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Lönnerdal, B. (1991). Lactoferrin Binding to its Intestinal Receptor. In: Mestecky, J., Blair, C., Ogra, P.L. (eds) Immunology of Milk and the Neonate. Advances in Experimental Medicine and Biology, vol 310. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3838-7_17
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DOI: https://doi.org/10.1007/978-1-4615-3838-7_17
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